Žučna so sulfotransferaza
| žučna so sulfotransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifikatori | |||||||||
| EC broj | 2.8.2.14 | ||||||||
| CAS broj | 65802-92-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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žučna so sulfotransferaza (EC 2.8.2.14, BAST I, žučna kiselina:3'-fosfoadenozin-5'-fosfosulfat sulfotransferaza, žučna so:3'fosfoadenozin-5'-fosfosulfat:sulfotransferaza, žučno kiselinska sulfotransferaza I, glikolithoholatna sulfotransferaza) je enzim sa sistematskim imenom 3'-fosfoadenilil-sulfat:glikolitoholat sulfotransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) 3'-fosfoadenilil sulfat + glikolithoholat adenozin 3',5'-bisfosfat + glikolithoholat 3-sulfat
- (2) 3'-fosfoadenilil sulfat + taurolithoholat adenozin 3',5'-bisfosfat + taurolithoholat sulfat
Formiranje sulfat estara žučne kiseline je esencijalni korak u prevenciji toksičnosti monohidroksi žučne kiseline kod mnogih vrsta.
Reference
- ↑ Chen, L.-J., Bolt, R.J. and Admirand, W.H. (1977). „Enzymatic sulfation of bile salts. Partial purification and characterization of an enzyme from rat liver that catalyzes the sulfation of bile salts”. Biochim. Biophys. Acta 480: 219-227. PMID 831833.
- ↑ Barnes, S., Waldrop, R., Crenshaw, J., King, R.J. and Taylor, K.B. (1986). „Evidence for an ordered reaction mechanism for bile salt: 3′phosphoadenosine-5′-phosphosulfate: sulfotransferase from rhesus monkey liver that catalyzes the sulfation of the hepatotoxin glycolithocholate”. J. Lipid Res. 27: 1111-1123. PMID 3470420.
- ↑ Barnes, S., Buchina, E.S., King, R.J., McBurnett, T. and Taylor, K.B. (1989). „Bile acid sulfotransferase I from rat liver sulfates bile acids and 3-hydroxy steroids: purification, N-terminal amino acid sequence, and kinetic properties”. J. Lipid Res. 30: 529-540. PMID 2754334.
- ↑ Russell, D.W. (2003). „The enzymes, regulation, and genetics of bile acid synthesis”. Annu. Rev. Biochem. 72: 137-174. PMID 12543708.
Literatura
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.
Spoljašnje veze
- MeSH Bile-salt+sulfotransferase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
